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J. Biol. Chem., Vol. 281, Issue 3, 1670-1679, January 20, 2006

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Streptococcal Protein FOG, a Novel Matrix Adhesin Interacting with Collagen I in Vivo^*

From the Department of Clinical Sciences, Section for Clinical and Experimental Infectious Medicine, Biomedical Center, Lund University, S-22184 Lund, Sweden

Group G streptococcus (GGS) is a human pathogen of emerging clinical significance. It causes skin and soft tissue infections, occasionally resulting in life-threatening conditions such as sepsis and necrotizing fasciitis. We recently identified FOG, a novel surface protein of GGS with fibrinogen binding and immune evasion properties. Here we investigated the role of FOG in streptococcal primary adhesion to host tissue. A FOG-expressing clinical isolate adhered more efficiently to human skin biopsies ex vivo and to the murine dermis in vivo than a FOG-deficient strain. Scanning and transmission electron microscopy of skin specimens exhibited that this property was assigned to the ability of FOG to interact with collagen I, a major interstitial component of the dermis. Overlay experiments with human skin extracts and radiolabeled FOG followed by matrix-assisted laser desorption/ionization time of flight mass spectrometry analysis identified both the 1- and 2-chains of collagen I as targets for FOG. Transmission electron microscopy of the molecular complexes revealed thread-like FOG molecules binding via their NH₂ termini to distinct sites on collagen I monomers and fibrils. The results demonstrate that FOG is important for GGS adhesion in vivo, implying a pathogenic role for this surface protein.

Received for publication, June 22, 2005 , and in revised form, November 7, 2005.

^* This work was supported by Swedish Research Council Project 7480, the Crafoordska, Magnus Bergvall, Greta & Johan Kocks, the Tore Nilsson, and Alfred Österlund Foundations, the Royal Physiographic Society and, Hansa Medical AB. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to this work.

² Supported by the Anna Greta Crafoord Foundation.

³ To whom correspondence may be addressed. Tel.: 46-46-2228569; Fax: 46-46-157756; E-mail: inga-maria.frick{at}med.lu.se. ⁴ To whom correspondence may be addressed. Tel.: 46-46-2220741; Fax: 46-46-157756; E-mail: matthias.morgelin{at}med.lu.se.

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